1- Biological Molecules Flashcards

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1
Q

monomer=

A

smaller units from which larger molecules (polymers) are made

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2
Q

polymers are held together by=

A

covalent bonds

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3
Q

monomer e.g.s

A

amino acids, nucleotides, monosaccharides

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4
Q

condensation reactions=

A

joining of 2 molecules by forming a chemical bond and eliminating 1 x H20

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5
Q

hydrolysis reaction=

A

breaking of a chemical bond between 2 molecules & involves addition of 1xH20

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6
Q

monosaccharide

A

monomers from which larger carbohydrates are made

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7
Q

monosaccharides e.g.s

A

glucose, galactose, fructose

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8
Q

Polysaccharides are held together by:

A

glycosidic bonds

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9
Q

disaccharides=

A
  • maltose (glucose+glucose)
  • sucrose (glucose+fructose)
  • lactose (glucose + galactose)
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10
Q

what are the 2 isomers of glucose?

A
  • a-glucose

- B-glucose

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11
Q

what is an isomer?

A

two or more compounds with the same molecular formula, but different arrangement of atoms

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12
Q

a vs b arrangement

A

a b

H O H H O H

HO OH HO H

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13
Q

which polysaccharide(s) are formed from a condensation of a-glucose?

A

glycogen & starch

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14
Q

which polysaccharide(s) are formed from a condensation reaction of B-glucose?

A

cellulose

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15
Q

polysaccharide features (2)

A
  • can be branched or unbranched

- chain may contain different types of monosaccharides

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16
Q

Starch- functions (2)

A
  • main energy storage in plants (in seeds)
  • can act as food source for humans
  • broken down into glucose by plants when they need energy
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17
Q

Starch- features (1)

A
  • does not change water potential in a cell because its insoluble in water
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18
Q

2 types of starch =

A
  1. amylose

2. amylopectin

19
Q

amylose vs amylopectin

A
amylose= unbranched, good for energy storage
amylopectin= branched, good for energy release
20
Q

glycogen structure (2)

A
  • compact (so good storage molecule)

- highly branched (so can be easily converted to glucose)

21
Q

cellulose structure=

A
  • long chain of B-glucose

- B-glucose molecules linked by glycosidic bonds to form LINEAR cellulose chains that are unbranched

22
Q

what are myofibrils

A

strong fibres made up of many cellulose chains that are held together by H bonds

23
Q

how does cellulose provide structural support to plants

A

because of the strength of myofibril fibres they are composed of

24
Q

digestion of cellulose=

A
  • broken down by human digestive enzymes

- herbivores can digest cellulose rich plant material

25
Q

Benedicts test for R sugars

A
  1. place 2ml of substance in boiling tube
  2. add 10 drops of Benedict’s solution
  3. Place in boiling water for 3-5 minutes
  4. If G/Y= some RS, If O/R= moderate RS, if Brick red= large amounts of RS
26
Q

Benedicts test for NR sugars=

A
  1. Do benedict’s (will be - result)
  2. Boil in dilute HCL (to hydrolyse NRs)
  3. Neutralise solution by adding sodium hydrogen carbonate
  4. Repeat Benedict’s (will be + result)
27
Q

Triglyceride structure=

A

1x glycerol
3x fatty acid
held together by ester bonds

27
Q

Triglyceride structure=

A

1x glycerol
3x fatty acid
held together by ester bonds

27
Q

Triglyceride structure=

A

1x glycerol
3x fatty acid
held together by ester bonds

28
Q

Phospholipid structure=

A

1x glycerol backbone
2x fatty acid
1x phosphate group

29
Q

amino acid structure=

A
NH2= (an amino group)
COOH= (a carboxyl group)
H= (H atom)
R= (side group)
30
Q

which structure of proteins have ionic bonding

A

tertiary structure

31
Q

What are dispulphide bridges=

A

covalent bonds within proteins containing C amino acids

32
Q

Protein- primary structure=

A

order of amino acids in polypeptide

33
Q

protein- secondary structure=

A
  • Primary polypeptide FOLDS and aa form H bonds with other AA
  • This causes the protein to fold or coil
  • mainly alpha-helix or beta pleated sheet arrangement
34
Q

protein-tertiary structure=

A
  • Secondary polypeptide FOLDS further to form a tertiary structure
  • interations between R groups create the tertiary structure
  • this is usually coiled or folded
  • Holding tertiary structure can be ionic bonds, H bonds and disulphide bridges
35
Q

Protein- Quaternary structure=

A

when multiple 3D polypeptides (subunits) can come together to form a complex, quaternary structure

36
Q

Main protein function e.g.s (3)

A
  • structural proteins
  • enzymes
  • antibodies
37
Q

Biuret test=

A
  1. Add sample to distilled water & biuret solution
  2. Shake solution & leave upright for 5 mins
  3. Observe colour: if PURPLE- protein is present
38
Q

Will the biuret test give a + result if free floating AA are in it?

A

No, they must be joined by peptide bonds to give + result

39
Q

Induced fit model=

A

As enzyme & substrate come together, this interaction causes a small shift in enzymes structure < this shift means enzyme & substrate can bind to form an E-S complex & catalyse a reaction

40
Q

specificity of enzymes determined by= (2)

A
  • active site

- environmental factors (temp, pH)

41
Q

Factors affecting rate of enzyme action (5)

A
  • temp
  • pH
  • competitive & non-competitive inhibitors
  • enzyme conc
  • substrate conc
42
Q

Formula for calculating H+ conc=

A

pH= log10 [H+]